The effect of neutral salt anions on the oxidative deamination activity of plant glutamate dehydrogenase
- 1 January 1978
- journal article
- conference paper
- Published by Springer Nature in Planta
- Vol. 138 (2), 161-165
- https://doi.org/10.1007/bf00391173
Abstract
Increasing concentrations of anions of the Hofmeister series decrease the activity of highly purified glutamate dehydrogenase (EC 1.4.1.2.) from Pisum sativum L. The extent of the inactivation, as estimated by the ion concentration which causes a 50% transformation of the native form to the low activity form of the enzyme (approximately “halfmaximal activity”), follows the ranking Cl−−−3 − −. Sulfate has a slightly activating effect. At salt concentrations higher than 1 M (with SCN− higher than 200 mM), the activity decreases to a value from 3–6% of the initial activity and remains then stable over a wide range of higher anion concentrations. From kinetic investigations it is seen that the treatment of the enzyme with anions decreases the affinity for the cosubstrate NAD+ and the substrate L-glutamate (K M-values increased) and also increases the dissociation constant for NAD+. The salt induced inactivation is reversible by dilution. From a mathematical treatment of the kinetic data of the inactivation, it is seen that increasing concentrations of the anions exert cooperative effects on the inactivation process.Keywords
This publication has 14 references indexed in Scilit:
- The effect of ions on the enzymatic properties of beef‐liver glutamate dehydrogenaseBiopolymers, 1977
- Studies of Glutamate Dehydrogenase. Regulation of Glutamate Dehydrogenase from Candida utilis by a pH and Temperature‐Dependent Conformational TransitionEuropean Journal of Biochemistry, 1976
- Über den Reaktionsmechanismus pflanzlicher Glutamatdehydrogenase und die Regulation der Aktivität durch Adenosinphosphate, die Energieladung und IonenPlanta, 1975
- Slow conformational changes of a Neurospora glutamate dehydrogenase studied by protein fluorescenceBiochemical Journal, 1974
- The Interaction of Chaotropic Anions with Proteins at Acid pHEuropean Journal of Biochemistry, 1973
- Biological functions of multistable proteinsJournal of Theoretical Biology, 1973
- Sind die multiplen Formen der Glutamatdehydrogenase aus Erbsenkeimlingen Conformer?Planta, 1972
- Allosterische Regulation der Aktivität der Glutamatdehydrogenase aus Erbsenkeimlingen durch das Substrat α-KetoglutarsäurePlanta, 1971
- Ion effects on the solution structure of biological macromoleculesAccounts of Chemical Research, 1969
- SOLUBILIZATION OF PARTICULATE PROTEINS AND NONELECTROLYTES BY CHAOTROPIC AGENTSProceedings of the National Academy of Sciences, 1969